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1PKY

PYRUVATE KINASE FROM E. COLI IN THE T-STATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0006950biological_processresponse to stress
A0009408biological_processresponse to heat
A0016020cellular_componentmembrane
A0030955molecular_functionpotassium ion binding
A0042802molecular_functionidentical protein binding
A1902912cellular_componentpyruvate kinase complex
B0000287molecular_functionmagnesium ion binding
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0006950biological_processresponse to stress
B0009408biological_processresponse to heat
B0016020cellular_componentmembrane
B0030955molecular_functionpotassium ion binding
B0042802molecular_functionidentical protein binding
B1902912cellular_componentpyruvate kinase complex
C0000287molecular_functionmagnesium ion binding
C0004743molecular_functionpyruvate kinase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006096biological_processglycolytic process
C0006950biological_processresponse to stress
C0009408biological_processresponse to heat
C0016020cellular_componentmembrane
C0030955molecular_functionpotassium ion binding
C0042802molecular_functionidentical protein binding
C1902912cellular_componentpyruvate kinase complex
D0000287molecular_functionmagnesium ion binding
D0004743molecular_functionpyruvate kinase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006096biological_processglycolytic process
D0006950biological_processresponse to stress
D0009408biological_processresponse to heat
D0016020cellular_componentmembrane
D0030955molecular_functionpotassium ion binding
D0042802molecular_functionidentical protein binding
D1902912cellular_componentpyruvate kinase complex
Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IhIISKIENqEGL
ChainResidueDetails
AILE215-LEU227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
ATHR278
AGLU314
ALYS220
AARG32
AARG73
ASER312

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
BTHR278
BGLU314
BLYS220
BARG32
BARG73
BSER312

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
CTHR278
CGLU314
CLYS220
CARG32
CARG73
CSER312

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
DTHR278
DGLU314
DLYS220
DARG32
DARG73
DSER312

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PDB entries from 2026-03-25

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